STAP1_MOUSE
ID STAP1_MOUSE Reviewed; 297 AA.
AC Q9JM90; A6H6C6; Q3TRM1; Q6PES6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Signal-transducing adaptor protein 1;
DE Short=STAP-1;
DE AltName: Full=Stem cell adaptor protein 1;
GN Name=Stap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION,
RP INTERACTION WITH KIT AND CSF1R, AND TISSUE SPECIFICITY.
RX PubMed=10679268; DOI=10.1006/bbrc.2000.2223;
RA Masuhara M., Nagao K., Nishikawa M., Sasaki M., Yoshimura A., Osawa M.;
RT "Molecular cloning of murine STAP-1, the stem-cell-specific adaptor protein
RT containing PH and SH2 domains.";
RL Biochem. Biophys. Res. Commun. 268:697-703(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-170, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as an adapter molecule downstream of KIT in the
CC proliferation or differentiation of hematopoietic stem cells.
CC {ECO:0000269|PubMed:10679268}.
CC -!- SUBUNIT: Interacts with URI1; the interaction is phosphorylation-
CC dependent occurs in a growth-dependent manner (By similarity).
CC Interacts with KIT and CSF1R. {ECO:0000250,
CC ECO:0000269|PubMed:10679268}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000305}.
CC Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JM90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JM90-2; Sequence=VSP_013399, VSP_013400;
CC -!- TISSUE SPECIFICITY: Expression restricted to the bone marrow.
CC {ECO:0000269|PubMed:10679268}.
CC -!- PTM: Phosphorylated on tyrosine by TEC. Phosphorylated on tyrosine by
CC KIT. {ECO:0000250}.
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DR EMBL; AB036058; BAA92531.1; -; mRNA.
DR EMBL; AK041474; BAC30953.1; -; mRNA.
DR EMBL; AK162655; BAE37007.1; -; mRNA.
DR EMBL; BC057898; AAH57898.1; -; mRNA.
DR EMBL; BC145828; AAI45829.1; -; mRNA.
DR EMBL; BC145830; AAI45831.1; -; mRNA.
DR CCDS; CCDS19377.1; -. [Q9JM90-1]
DR RefSeq; NP_001297568.1; NM_001310639.1.
DR RefSeq; NP_064376.1; NM_019992.4. [Q9JM90-1]
DR RefSeq; XP_006535224.1; XM_006535161.3.
DR AlphaFoldDB; Q9JM90; -.
DR SMR; Q9JM90; -.
DR BioGRID; 208177; 7.
DR STRING; 10090.ENSMUSP00000031171; -.
DR iPTMnet; Q9JM90; -.
DR PhosphoSitePlus; Q9JM90; -.
DR SwissPalm; Q9JM90; -.
DR EPD; Q9JM90; -.
DR MaxQB; Q9JM90; -.
DR PaxDb; Q9JM90; -.
DR PeptideAtlas; Q9JM90; -.
DR PRIDE; Q9JM90; -.
DR ProteomicsDB; 258748; -. [Q9JM90-1]
DR ProteomicsDB; 258749; -. [Q9JM90-2]
DR Antibodypedia; 24136; 217 antibodies from 22 providers.
DR DNASU; 56792; -.
DR Ensembl; ENSMUST00000198435; ENSMUSP00000143251; ENSMUSG00000029254. [Q9JM90-1]
DR GeneID; 56792; -.
DR KEGG; mmu:56792; -.
DR UCSC; uc008xxf.1; mouse. [Q9JM90-2]
DR UCSC; uc008xxg.1; mouse. [Q9JM90-1]
DR CTD; 26228; -.
DR MGI; MGI:1926193; Stap1.
DR VEuPathDB; HostDB:ENSMUSG00000029254; -.
DR eggNOG; ENOG502RZ9C; Eukaryota.
DR GeneTree; ENSGT00530000063841; -.
DR HOGENOM; CLU_043957_1_0_1; -.
DR InParanoid; Q9JM90; -.
DR OMA; PACFFDV; -.
DR OrthoDB; 70229at2759; -.
DR PhylomeDB; Q9JM90; -.
DR TreeFam; TF332087; -.
DR BioGRID-ORCS; 56792; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Stap1; mouse.
DR PRO; PR:Q9JM90; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JM90; protein.
DR Bgee; ENSMUSG00000029254; Expressed in granulocyte and 74 other tissues.
DR ExpressionAtlas; Q9JM90; baseline and differential.
DR Genevisible; Q9JM90; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; IPI:BHF-UCL.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:BHF-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
DR GO; GO:0030099; P:myeloid cell differentiation; TAS:MGI.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IMP:BHF-UCL.
DR GO; GO:1902227; P:negative regulation of macrophage colony-stimulating factor signaling pathway; IMP:BHF-UCL.
DR GO; GO:1904140; P:negative regulation of microglial cell migration; IMP:BHF-UCL.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:BHF-UCL.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; IMP:BHF-UCL.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; IDA:BHF-UCL.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
DR CDD; cd10403; SH2_STAP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR039111; STAP1/STAP2.
DR InterPro; IPR035877; STAP1_SH2.
DR PANTHER; PTHR16186; PTHR16186; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..297
FT /note="Signal-transducing adaptor protein 1"
FT /id="PRO_0000072238"
FT DOMAIN 25..121
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 179..273
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 271..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT VAR_SEQ 122..127
FT /note="LTVPQH -> VIRFPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013399"
FT VAR_SEQ 128..297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013400"
SQ SEQUENCE 297 AA; 34628 MW; 8033C606990AAA75 CRC64;
MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLVKRSDHQ EYKHYWTELR GTTLFFYTDK
KSTIYVGKLD IIDLVCLTGQ HSTEKNCAKF TLVLPKEEVH VKTENTESGE EWRGFILTVT
ELTVPQHVSL LPGQVIRLHE VLEREKKRRI ETDQLPLMPP EKEKEPVQDY ADVLNPLPEC
FYAVSRKEAT AMLEKNPSWG NMILRPGSDS KNYSITIRQE IEMPRIKHFK VTRTGNNYTI
ELEKPVTLPN LFSVIDYFVK ETRGNLRPFI HSADDNFGQD PNIEDRSEKF KKNPHNA
